Evidence map›Paper›PMID 34198590›Full record

ArticleCancers2021

A Novel Protein-Protein Interaction between RSK3 and IκBα and a New Binding Inhibitor That Suppresses Breast Cancer Tumorigenesis.

Hee-Sub Yoon, Sung Hoon Choi, Jung-Hyun Park, Jin-Young Min, Ju-Yong Hyon, Yeji Yang, Sejin Jung, Jae-Young Kim, Nam Doo Kim, Ji Hoon Lee and 3 more

Open access · goldAbstract read
In one paragraph

Article in Cancers, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 26% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 14 citations in OpenAlex.

  1. RiSKs in Computational Modeling of Isoform-Selective RSK Inhibitors.Journal of chemical information and modeling · 2025
    Review
  2. Article
  3. RSK3 switches cell fate: from stress-induced senescence to malignant progression.Journal of experimental & clinical cancer research : CR · 2023
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 5 institutions in 1 country.

Hee-Sub YoonResearch Center for Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Cheongju 28119, Korea.ORCID 0000-0002-3355-0354
Sung Hoon ChoiResearch Center for Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Cheongju 28119, Korea.
Jung-Hyun ParkResearch Center for Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Cheongju 28119, Korea.
Jin-Young MinResearch Center for Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Cheongju 28119, Korea.
Ju-Yong HyonResearch Center for Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Cheongju 28119, Korea.
Yeji YangResearch Center for Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Cheongju 28119, Korea.
Sejin JungNew Drug Development Center, Daegu Gyeoungbuk Medical Innovation Foundation DGMIF, Daegu 41061, Korea.ORCID 0000-0002-3012-574X
Jae-Young KimGraduate School of Analytical Science and Technology (GRAST), Chungnam National University, Daejeon 34134, Korea.
Nam Doo KimNew Drug Development Center, Daegu Gyeoungbuk Medical Innovation Foundation DGMIF, Daegu 41061, Korea.
Ji Hoon LeeNew Drug Development Center, Daegu Gyeoungbuk Medical Innovation Foundation DGMIF, Daegu 41061, Korea.
Eun Hee HanResearch Center for Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Cheongju 28119, Korea.ORCID 0000-0002-0137-0156
Sung-Gil ChiDepartment of Life Sciences, Korea University, Seoul 02841, Korea.ORCID 0000-0003-4643-9003
Young-Ho ChungResearch Center for Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Cheongju 28119, Korea.ORCID 0000-0002-1779-0657
Korea Basic Science Institute · KRDaegu-Gyeongbuk Medical Innovation Foundation · KRChungnam National University · KRKorea University · KRYonsei University · KR

Funding

Korea Basic Science Institute funded by the Ministry of Science, ICT D38404, C38115National Research Foundation of Korea Grant funded by the Korean Government (MSIT) 2013R1A6A9067028
6 · The paper itself

Abstract

Multiple cancer-related biological processes are mediated by protein-protein interactions (PPIs). Through interactions with a variety of factors, members of the ribosomal S6 kinase (RSK) family play roles in cell cycle progression and cell proliferation. In particular, RSK3 contributes to cancer viability, but the underlying mechanisms remain unknown. We performed a kinase library screen to find IκBα PPI binding partners and identified RSK3 as a novel IκBα binding partner using a cell-based distribution assay. In addition, we discovered a new PPI inhibitor using mammalian two-hybrid (MTH) analysis. We assessed the antitumor effects of the new inhibitor using cell proliferation and colony formation assays and monitored the rate of cell death by FACS apoptosis assay. IκBα is phosphorylated by the active form of the RSK3 kinase. A small-molecule inhibitor that targets the RSK3/IκBα complex exhibited antitumor activity in breast cancer cells and increased their rate of apoptosis. RSK3 phosphorylation and RSK3/IκBα complex formation might be functionally important in breast tumorigenesis. The RSK3/IκBα-specific binding inhibitor identified in this study represents a lead compound for the development of new anticancer drugs.

Indexed as

binding inhibitionbreast cancercell-based unidentified protein interaction discovery (CUPID)IκBαprotein-protein interaction (PPI)RSK3 (RPS6KA2)

Identifiers

PMID34198590
PMCPMC8231827
OpenAlexW3166485299

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.